[HTML][HTML] Folding of prion protein to its native α-helical conformation is under kinetic control
IV Baskakov, G Legname, SB Prusiner… - Journal of Biological …, 2001 - ASBMB
The recombinant mouse prion protein (MoPrP) can be folded either to a monomeric α-helical
or oligomeric β-sheet-rich isoform. By using circular dichroism spectroscopy and size-
exclusion chromatography, we show that the β-rich isoform of MoPrP is thermodynamically
more stable than the native α-helical isoform. The conformational transition from the α-
helical to β-rich isoform is separated by a large energetic barrier that is associated with
unfolding and with a higher order kinetic process related to oligomerization. Under partially …
or oligomeric β-sheet-rich isoform. By using circular dichroism spectroscopy and size-
exclusion chromatography, we show that the β-rich isoform of MoPrP is thermodynamically
more stable than the native α-helical isoform. The conformational transition from the α-
helical to β-rich isoform is separated by a large energetic barrier that is associated with
unfolding and with a higher order kinetic process related to oligomerization. Under partially …